RHG29_MOUSE
ID RHG29_MOUSE Reviewed; 1266 AA.
AC Q8CGF1; Q3V135; Q7TMW2; Q8BLJ2; Q8BLR8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rho GTPase-activating protein 29;
DE AltName: Full=Rho-type GTPase-activating protein 29;
GN Name=Arhgap29;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C3H/He, and FVB/N; TISSUE=Mammary tumor, and Mesenchymal stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-176 AND SER-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-179; SER-190;
RP SER-521 AND SER-1149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, INTERACTION WITH RASIP1, AND DEVELOPMENTAL STAGE.
RX PubMed=21396893; DOI=10.1016/j.devcel.2011.02.010;
RA Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E.,
RA Cleaver O.;
RT "Blood vessel tubulogenesis requires Rasip1 regulation of GTPase
RT signaling.";
RL Dev. Cell 20:526-539(2011).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Has strong activity toward RHOA, and
CC weaker activity toward RAC1 and CDC42. May act as a specific effector
CC of RAP2A to regulate Rho (By similarity). In concert with RASIP1,
CC suppresses RhoA signaling and dampens ROCK and MYH9 activities in
CC endothelial cells and plays an essential role in blood vessel
CC tubulogenesis. {ECO:0000250, ECO:0000269|PubMed:21396893}.
CC -!- SUBUNIT: Interacts with PTPN13/PTPL1. Interacts with RAP2A via its
CC coiled coil domain (By similarity). Interacts with RASIP1.
CC {ECO:0000250, ECO:0000269|PubMed:21396893}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CGF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGF1-2; Sequence=VSP_031060;
CC -!- DEVELOPMENTAL STAGE: In embryos, present in the endothelial cells of
CC the paired aortae during vasculogenesis (at protein level).
CC {ECO:0000269|PubMed:21396893}.
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DR EMBL; AK043637; BAC31603.2; -; mRNA.
DR EMBL; AK044979; BAC32168.2; -; mRNA.
DR EMBL; AK132716; BAE21318.1; -; mRNA.
DR EMBL; BC040387; AAH40387.1; -; mRNA.
DR EMBL; BC052858; AAH52858.1; -; mRNA.
DR CCDS; CCDS17807.1; -. [Q8CGF1-1]
DR RefSeq; NP_766113.1; NM_172525.2. [Q8CGF1-1]
DR RefSeq; XP_006501351.1; XM_006501288.3.
DR AlphaFoldDB; Q8CGF1; -.
DR SMR; Q8CGF1; -.
DR BioGRID; 229497; 9.
DR STRING; 10090.ENSMUSP00000044624; -.
DR iPTMnet; Q8CGF1; -.
DR PhosphoSitePlus; Q8CGF1; -.
DR jPOST; Q8CGF1; -.
DR MaxQB; Q8CGF1; -.
DR PaxDb; Q8CGF1; -.
DR PeptideAtlas; Q8CGF1; -.
DR PRIDE; Q8CGF1; -.
DR ProteomicsDB; 255332; -. [Q8CGF1-1]
DR ProteomicsDB; 255333; -. [Q8CGF1-2]
DR Antibodypedia; 19948; 106 antibodies from 18 providers.
DR DNASU; 214137; -.
DR Ensembl; ENSMUST00000037958; ENSMUSP00000044624; ENSMUSG00000039831. [Q8CGF1-1]
DR GeneID; 214137; -.
DR KEGG; mmu:214137; -.
DR UCSC; uc008reh.1; mouse. [Q8CGF1-1]
DR CTD; 9411; -.
DR MGI; MGI:2443818; Arhgap29.
DR VEuPathDB; HostDB:ENSMUSG00000039831; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_2_0_1; -.
DR InParanoid; Q8CGF1; -.
DR OMA; QMIFDTP; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q8CGF1; -.
DR TreeFam; TF351450; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 214137; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Arhgap29; mouse.
DR PRO; PR:Q8CGF1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CGF1; protein.
DR Bgee; ENSMUSG00000039831; Expressed in cumulus cell and 232 other tissues.
DR ExpressionAtlas; Q8CGF1; baseline and differential.
DR Genevisible; Q8CGF1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1266
FT /note="Rho GTPase-activating protein 29"
FT /id="PRO_0000317583"
FT DOMAIN 192..462
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 673..888
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 614..659
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1266
FT /note="Interaction with PTPN13/PTPL1"
FT /evidence="ECO:0000250"
FT COILED 296..418
FT /evidence="ECO:0000255"
FT COMPBIAS 482..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT VAR_SEQ 379..1035
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031060"
FT CONFLICT 165
FT /note="I -> T (in Ref. 2; AAH52858)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="N -> D (in Ref. 1; BAE21318)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> L (in Ref. 1; BAE21318)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="E -> G (in Ref. 1; BAC31603)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088
FT /note="Q -> R (in Ref. 2; AAH52858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1266 AA; 142341 MW; 96687B52C3D229D2 CRC64;
MIAHKQKKAK KKRVWASGQP SAAITTSEMG LKSVSSSSSF DPEYIKELVN DVRKFSHMLL
YLKEAILSDC FKEVIHIRLD ELLRVLKSIL SKHQNLSSVD LQSAAEVLTA KVKAVNFTEV
NEENKNDIFR EVFSSIETLA FTFGNILTNF LMGDVGSDSI LRLPISRESK SFENISVDSV
DLPHEKGNFS PIELDNLLLK NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNI
VKLAEATRSS IGIQEFMPLQ SLFTNALLSD IHSSHLLQQT IAALQANKFV QPLLGRKNEM
EKQRKEIKDL WKQQQNKLLE TETALKKAKL LCMQRQDEYE KAKSSMFRAE EEQLSSSVGL
AKNLNKQLEK RRRLEEEALQ KVEEANEHYK VCVTNVEERR NDLENTKREI LTQLRTLVFQ
CDLTLKAVTV NLFHMQQLQA ASLANSLQSL CDSAKLYDPG QEYSEFVKAT SSSELEEKVD
GNVNKQMTNS PQTSGYEPAD SLEDVARLPD SCHKLEEDRC SNSADMTGPS FVRSWKFGMF
SDSESTGGSS ESRSLDSESI SPGDFHRKLP RTPSSGTMSS ADDLDEREPP SPSEAGPNSL
GAFKKTLMSK AALTHKFRKL RSPTKCRDCD GIVMFPGVEC EECLLVCHRK CLENLVIICG
HQKLQGKMHI FGAEFIQVAK KEPDGIPFVL KICASEIENR ALCLQGIYRV CGNKIKTEKL
CQALENGMHL VDISEFSSHD ICDVLKLYLR QLPEPFILFR LYKEFIDLAK EIQHVNEEQE
AKKDSPEDKK HPHVSIEVNR ILLKSKDLLR QLPASHFNSL HYLIAHLRRV VDHAEENKMN
SKNLGVIFGP TLIRPRPTTA PVTISSLAEY SNQARLVEFL ITYSQKIFDG SLQPQAVVIS
NTGAVAPQVD QGYLPKPLLS PDERDTDHSM KPLFFSSKED IRSSDCESKS FELTTSFEES
ERRQNALGKC DAPLLDNKVH LLFDQEHESA SQKMEDVCKS PKLLLLKSNR AANSVQRHTP
RTKMRPVSLP VDRLLLLASS PTERSSRDVG NVDSDKFGKN PAFEGLHRKD NSNTTRSKVN
GFDQQNVQKS WDTQYVRNNF TAKTTMIVPS AYPEKGLTVN TGNNRDHPGS KAHAEPARAA
GDVSERRSSD SCPATAVRAP RTLQPQHWTT FYKPPNPTFS VRGTEEKTAL PSIAVPPVLV
HAPQIHVTKS DPDSEATLAC PVQTSGQPKE SSEEPALPEG TPTCQRPRLK RMQQFEDLED
EIPQFV
